Open AccessX‐ray Absorption Spectroscopy Study of Native and Phenylphosphorodiamidate‐Inhibited Bacillus pasteurii Urease
Author(s) -
Benini Stefano,
Ciurli Stefano,
Nolting Hans F.,
Mangani Stefano
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.0061u.x
Subject(s) - urease , x ray absorption spectroscopy , chemistry , nickel , atomic absorption spectroscopy , spectroscopy , nuclear chemistry , histidine , absorption (acoustics) , enterobacter aerogenes , enzyme , absorption spectroscopy , crystallography , biochemistry , materials science , organic chemistry , escherichia coli , physics , gene , quantum mechanics , composite material
X‐ray absorption spectroscopy (XAS) has been applied to urease from Bacillus pasteurii , a highly ureolytic soil bacterium, with the aim of elucidating the structural details of the nickel‐containing active site. The results indicate the presence of octahedrally coordinated Ni 2+ , in a sphere of six N/O donors at an average distance of 0.203 nm. An average of two histidine residues are bound to nickel. The experimental evidence suggests direct binding of the urease inhibitor phenylphosphorodiamidate to Ni 2+ . These spectroscopic results are in agreement with previous findings on both plant and microbial ureases, but differ in some respect from the results obtained by X‐ray crystallography analysis of Klebsiella aerogenes urease.